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Originally published as Biophys J. BioFAST on November 11, 2005.
doi:10.1529/biophysj.105.060442
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Biophysical Journal 90:1055-1063 (2006)
© 2006 The Biophysical Society

Change in Rigidity in the Activated Form of the Glucose/Galactose Receptor from Escherichia coli: A Phenomenon that Will Be Key to the Development of Biosensors

Igor Sokolov * {dagger}, Venkatesh Subba-Rao * and Linda A. Luck {dagger}

* Department of Physics, and {dagger} Department of Chemistry, Clarkson University, Potsdam, New York 13699

Correspondence: Address reprint requests to Igor Sokolov, Dept. of Physics, Clarkson University, PO Box 5820, Potsdam, NY 13699-5820. Tel.: 315-268-2375; E-mail: sokolov{at}clarkson.edu.

Recently a periplasmic glucose/galactose binding protein, GGRQ26C, immobilized on a gold surface has been used as an active part of a glucose biosensor based on quartz microbalance technique. However the nature of the glucose detection was not clear. Here we have found that the receptor protein film immobilized on the gold surface increases its rigidity when glucose is added, which explains the unexpected detection signal. To study the rigidity change, we developed a new fast and simple method based on using atomic force microscopy (AFM) in tapping mode. The method was verified by explicit measurements of the Young's modulus of the protein film by conventional AFM methods. Since there are a host of receptors that undergo structural change when activated by ligand, AFM can play a key role in the development and/or optimization of biosensors based on rigidity changes in biomolecules.




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